topA Antibody

1. the CyaA(N600Y) mutant has a transcriptome indicative of increased CRP activity, pointing to an unknown role for CyaA and / or cAMP in gene expression..We show that the large scale transcriptomic changes in the topoisomerase I (FusA(A608E)-TopA(S180L)) mutant likely result from increased negative supercoiling in the cell. PMID: 29046437
2. Escherichia coli RecA physically interacts with topoisomerase I to modulate the chromosomal DNA supercoiling. PMID: 27001450
3. Structural study shows how the C-terminal domains of E. coli topoisomerase I bind single-stranded DNA to recognize the accumulation of negative supercoils in duplex DNA. PMID: 26490962
4. Antimicrobial susceptibility and SOS-dependent increase in mutation frequency are impacted by Escherichia coli topoisomerase I C-terminal point mutation. PMID: 26248366
5. Data indicate that transcription-coupled DNA supercoiling (TCDS) in topoisomerase I deficient (topA) is dependent on promoter strength. PMID: 23201416
6. Topoisomerase I relaxes DNA in slow processive runs but with short pauses before runs. PMID: 22923519
7. These data show unambiguously that Escherichia coli cells are not viable in the absence of DNA topoisomerase I without the presence of compensatory mutations. PMID: 22373098
8. essential function is related to transcription elongation, to inhibition of R-loop formation and to allowing the synthesis of full-length mRNAs PMID: 15458416
9. E. coli strains bearing topA mutations, introduced into the strains by DNA-mediated gene replacement, are viable at 37 or 42 degrees C without any compensatory mutations PMID: 15522872
10. analysis of topoisomerase I DNA cleavage activity PMID: 16159875
11. Catalytic roles of the conserved lysine and serine found at the active site of DNA topoisomerase I. PMID: 16582104
12. in response to oxidative stress, Fis binds the promoter region of topA PMID: 17233826
13. DNA of topA null mutants became relaxed rather than hypernegatively supercoiled following depletion of RNase HI activity. PMID: 18554330
14. The Asp-to-Asn substitutions at the TOPRIM domain residues can selectively decrease Mg(2+) binding affinity with minimal disruption of the active-site geometry, leading to trapping of the covalent complex with cleaved DNA and causing bacterial cell death. PMID: 19013470

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KEGG: ecj:JW1266

STRING: 316385.ECDH10B_1389